ID A0A1F7ZLI6_9EURO Unreviewed; 516 AA.
AC A0A1F7ZLI6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Ceramide glucosyltransferase {ECO:0000256|ARBA:ARBA00019988};
DE EC=2.4.1.80 {ECO:0000256|ARBA:ARBA00012699};
DE AltName: Full=Glucosylceramide synthase {ECO:0000256|ARBA:ARBA00031543};
DE AltName: Full=UDP-glucose ceramide glucosyltransferase {ECO:0000256|ARBA:ARBA00032575};
DE AltName: Full=UDP-glucose:N-acylsphingosine D-glucosyltransferase {ECO:0000256|ARBA:ARBA00031017};
GN ORFNames=ABOM_011079 {ECO:0000313|EMBL:OGM40304.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM40304.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM40304.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00004760}.
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC {ECO:0000256|ARBA:ARBA00006739}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGM40304.1}.
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DR EMBL; LYCR01000150; OGM40304.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7ZLI6; -.
DR STRING; 109264.A0A1F7ZLI6; -.
DR OrthoDB; 2786173at2759; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000179179; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008120; F:ceramide glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102769; F:dihydroceramide glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0043934; P:sporulation; IEA:UniProt.
DR InterPro; IPR025993; Ceramide_glucosylTrfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR12726; CERAMIDE GLUCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR12726:SF0; CERAMIDE GLUCOSYLTRANSFERASE; 1.
DR Pfam; PF13506; Glyco_transf_21; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OGM40304.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 389..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 463..481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 197..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 516 AA; 57893 MW; 49F914B1D49B64DA CRC64;
MLTVAQTNAA SNRWRYFLQR PRKSHSATAS DAPHVTAIRP VKGLEPNLYD CLASTFRQDY
PADKLTVYFC VASRSDPGYP TLQKLVSDFP HAGARIFIEE EDPLLQPDGE RIYNLGPNPK
IRNMSRAYRE AKGDIVWIID CNVWVGKGVC GRMVDRLCGL GATSGKKYKF VHHLPLVVDV
TSDASLTEEQ SALVESYTNG DADPSGDVSS APTISNHEQG TLATGGGCLE ELFLSSSHAK
MYTAINTVLI APCIVGKSNM FRRSHLDYLT TSSTDPHKRN PGIDYFSDNI CEDHLIGDLL
WKNRVREEKE NGERFGKHGM VFGDLAIQPV GNMSVGDYIA RRVRWLRVRK FTVLLATLVE
PGTESLLCSC YGAWGVTTSL AQFLQGKGFY CATYMTTWAA FFAFFFLSLA IWILTDWTLY
IKLHSAKSVE LDEDTPPFAR PPSHRLTRRT FLQWFSAWLG REFLALPIWI WAFYGGVTVT
WRNRRFRVGL DMKVREIGSD KTPLPDSKQA PASQGN
//
